Untangling a Structurally Resolved Protein Folding Intermediate

Abstract

A central challenge in protein biophysics is to decipher the structural features that give rise to the energetics of protein folding pathways and determine structural details of intermediates. A unique advantage of single-molecule force spectroscopy over classical thermodynamic methods of monitoring protein folding and unfolding transitions is that force spectroscopy effectively reduces the ensemble of possible conformational states to those whose unfolding trajectories share a common reaction coordinate experimentally controlled by the vector of applied force.